PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24429282-11	2014	Finally, depleting endogenous PIP2 with polyphosphoinositide phosphatase synaptojanin-1, known to disperse Syn-1A clusters, freed Syn-1A from Syn-1A clusters to bind SUR1, causing inhibition of KATP channels that could no longer be further inhibited by exogenous Syn-1A.	Phosphatidylinositol 4,5-Diphosphate	30-34	ATP binding cassette subfamily C member 8	Homo sapiens	166-170	
28092267-5	2017	Intricate interactions between TMD0, the loop following TMD0, and Kir6.2 near the proposed PIP2 binding site, and where ATP density is observed, suggest SUR1 may contribute to ATP and PIP2 binding to enhance Kir6.2 sensitivity to both.	Phosphatidylinositol 4,5-Diphosphate	91-95	ATP binding cassette subfamily C member 8	Homo sapiens	153-157	
28086082-6	2017	In another structural population, a putative co-purified phosphatidylinositol 4,5-bisphosphate (PIP2) molecule uncouples Kir6.2 from glibenclamide-bound SUR1.	Phosphatidylinositol 4,5-Diphosphate	57-94	ATP binding cassette subfamily C member 8	Homo sapiens	153-157	
28086082-6	2017	In another structural population, a putative co-purified phosphatidylinositol 4,5-bisphosphate (PIP2) molecule uncouples Kir6.2 from glibenclamide-bound SUR1.	Phosphatidylinositol 4,5-Diphosphate	96-100	ATP binding cassette subfamily C member 8	Homo sapiens	153-157	
24429282-3	2014	PIP2 also modifies Syn-1A clustering in plasma membrane (PM) that may alter Syn-1A actions on PM proteins like SUR1.	Phosphatidylinositol 4,5-Diphosphate	0-4	ATP binding cassette subfamily C member 8	Homo sapiens	111-115	
24429282-4	2014	Here, we assessed whether the actions of PIP2 on activating KATP channels is contributed by sequestering Syn-1A from binding SUR1.	Phosphatidylinositol 4,5-Diphosphate	41-45	ATP binding cassette subfamily C member 8	Homo sapiens	125-129	
24429282-5	2014	In vitro binding showed that PIP2 dose-dependently disrupted Syn-1A SUR1 complexes, corroborated by an in vivo Forster resonance energy transfer assay showing disruption of SUR1(-EGFP)/Syn-1A(-mCherry) interaction along with increased Syn-1A cluster formation.	Phosphatidylinositol 4,5-Diphosphate	29-33	ATP binding cassette subfamily C member 8	Homo sapiens	68-72	
24429282-8	2014	First, we showed that PIP2-insensitive Syn-1A-5RK/A mutant complex with SUR1 could not be disrupted by PIP2, consequently reducing PIP2 activation of KATP channels.	Phosphatidylinositol 4,5-Diphosphate	22-26	ATP binding cassette subfamily C member 8	Homo sapiens	72-76	
24429282-9	2014	Next, Syn-1A SUR1 complex modulation of KATP channels could be observed at a physiologically low PIP2 concentration that did not disrupt the Syn-1A SUR1 complex, compared with higher PIP2 concentrations acting directly on Kir6.2.	Phosphatidylinositol 4,5-Diphosphate	97-101	ATP binding cassette subfamily C member 8	Homo sapiens	13-17	
28092267-5	2017	Intricate interactions between TMD0, the loop following TMD0, and Kir6.2 near the proposed PIP2 binding site, and where ATP density is observed, suggest SUR1 may contribute to ATP and PIP2 binding to enhance Kir6.2 sensitivity to both.	Phosphatidylinositol 4,5-Diphosphate	184-188	ATP binding cassette subfamily C member 8	Homo sapiens	153-157	
24429282-12	2014	These results taken together indicate that PIP2 affects islet beta-cell KATP channels not only by its actions on Kir6.2 but also by sequestering Syn-1A to modulate Syn-1A availability and its interactions with SUR1 on PM.	Phosphatidylinositol 4,5-Diphosphate	43-47	ATP binding cassette subfamily C member 8	Homo sapiens	210-214	
21654216-0	2011	ATP activates ATP-sensitive potassium channels composed of mutant sulfonylurea receptor 1 and Kir6.2 with diminished PIP2 sensitivity.	Phosphatidylinositol 4,5-Diphosphate	117-121	ATP binding cassette subfamily C member 8	Homo sapiens	66-89	
21321069-0	2011	N-terminal transmembrane domain of SUR1 controls gating of Kir6.2 by modulating channel sensitivity to PIP2.	Phosphatidylinositol 4,5-Diphosphate	103-107	ATP binding cassette subfamily C member 8	Homo sapiens	35-39	
16373383-1	2006	ATP-sensitive K+ channels composed of the pore-forming protein Kir6.2 and the sulphonylurea receptor SUR1 are inhibited by ATP and activated by Phosphatidylinositol Bisphosphate (PIP2).	Phosphatidylinositol 4,5-Diphosphate	179-183	ATP binding cassette subfamily C member 8	Homo sapiens	101-105	
16373383-3	2006	Regulation of Kir6.2 by SUR1, however, is not well-understood, even though this process is ATP and PIP2 dependent.	Phosphatidylinositol 4,5-Diphosphate	99-103	ATP binding cassette subfamily C member 8	Homo sapiens	24-28	
16373383-8	2006	Based on macroscopic and single-channel data, we propose a model in which entry into the high-P(o) bursting state by the C166A mutation or by SUR1 depends on the interaction of PIP2 with R176 and R177 and, to a lesser extent, R54.	Phosphatidylinositol 4,5-Diphosphate	177-181	ATP binding cassette subfamily C member 8	Homo sapiens	142-146	
10435998-3	1999	Phosphatidylinositol 4, 5-bisphosphate (PIP(2)) profoundly antagonized ATP inhibition of K(ATP) channels expressed from cloned Kir6.2+SUR1 subunits, but also abolished high affinity tolbutamide sensitivity.	Phosphatidylinositol 4,5-Diphosphate	0-38	ATP binding cassette subfamily C member 8	Homo sapiens	134-138	
9804555-3	1998	It is reported here that phosphatidylinositol-4, 5-bisphosphate (PIP2) and phosphatidylinositol-4-phosphate (PIP) controlled ATP inhibition of cloned KATP channels (Kir6.2 and SUR1).	Phosphatidylinositol 4,5-Diphosphate	25-63	ATP binding cassette subfamily C member 8	Homo sapiens	176-180	
9804555-3	1998	It is reported here that phosphatidylinositol-4, 5-bisphosphate (PIP2) and phosphatidylinositol-4-phosphate (PIP) controlled ATP inhibition of cloned KATP channels (Kir6.2 and SUR1).	Phosphatidylinositol 4,5-Diphosphate	65-69	ATP binding cassette subfamily C member 8	Homo sapiens	176-180